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Prion protein biosynthesis

The cellular form of the prion protein, called PrP, is synthesized as a 253 amino acid precursor protein in humans (Figure 29. IB) (Prusiner, 1991). The N-terminal 22 amino acid residues serve as the signal peptide that allows insertion of the nascent PrP peptide into the secretory pathway during biosynthesis. The C-terminal 22 amino acid residues are involved in the covalent addition of the glycosylphosphatidylino-sitol (GPI) moiety to serine at amino acid 231 (i.e., Ser 9-The GPI anchor tethers PrP to the exhacellular side of the plasma membrane. PrP has two N-hnked glycosylation sites (Asn and Asn ) that are the sites of attachment of complex... [Pg.404]

Caughey B, Race RE, Ernst D, Buchmeier MJ, Chesebro B (1989) Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells. J Virol 63 175... [Pg.196]

Chakrabarti O, Ashok A, Hegde RS (2009) Prion protein biosynthesis and its emerging role in neurodegeneration. Trends Biochem Sci 34 287-295... [Pg.218]

See other pages where Prion protein biosynthesis is mentioned: [Pg.69]    [Pg.203]    [Pg.263]    [Pg.216]    [Pg.203]    [Pg.205]    [Pg.207]    [Pg.209]    [Pg.211]    [Pg.213]    [Pg.215]    [Pg.217]    [Pg.219]    [Pg.221]    [Pg.223]    [Pg.225]    [Pg.227]    [Pg.180]    [Pg.337]    [Pg.216]    [Pg.1853]    [Pg.629]    [Pg.596]    [Pg.2009]    [Pg.399]   


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